AC   MF_00219;
DC   Protein; auto
TR   HAMAP; MF_00219; -; 1; level=0
XX
Names: PyrC_classII
XX
ID   PYRC
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC;
XX
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC       to dihydroorotate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC         Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 3/3.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class II DHOase subfamily.
XX
DR   Pfam; PF01979; Amidohydro_1; 1; trigger=no
DR   PIRSF; PIRSF001237; DHOdimr; 1; trigger=no
DR   NCBIfam; TIGR00856; PyrC_dimer; 1; trigger=no
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1; trigger=no
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1; trigger=no
XX
KW   Hydrolase
KW   Metal-binding
KW   Pyrimidine biosynthesis
KW   Zinc
XX
GO   GO:0004151; F:dihydroorotase activity
GO   GO:0008270; F:zinc ion binding
GO   GO:0006221; P:pyrimidine nucleotide biosynthetic process
XX
FT   From: PYRC_ECOLI (P05020)
FT   BINDING         19..21
FT                   /ligand="substrate"
FT   Optional; Condition: H-[LFV]-R
FT   ACT_SITE        251
FT   Condition: D
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT   Condition: K
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT   Condition: K
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         45
FT                   /ligand="substrate"
FT   Optional; Condition: N
FT   BINDING         140
FT                   /ligand="substrate"
FT   Optional; Condition: H
FT   BINDING         223
FT                   /ligand="substrate"
FT   Optional; Condition: L
FT   BINDING         255
FT                   /ligand="substrate"
FT   Optional; Condition: H
FT   BINDING         267
FT                   /ligand="substrate"
FT   Optional; Condition: A
FT   MOD_RES         103
FT                   /note="N6-carboxylysine"
FT   Condition: K
XX
Size: 300-400;
Related: MF_00220;
Template: P05020; A6T7D6; B1IV40; P06204; Q8ZFU4;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Classification into subfamilies was done according to PubMed:24332717
XX
# Revision 1.40 2023/06/01
//